CA2598321A1 - Procede de detection differentielle d'une forme multimere a partir d'une forme monomere de polypeptides formant des multimeres - Google Patents
Procede de detection differentielle d'une forme multimere a partir d'une forme monomere de polypeptides formant des multimeres Download PDFInfo
- Publication number
- CA2598321A1 CA2598321A1 CA002598321A CA2598321A CA2598321A1 CA 2598321 A1 CA2598321 A1 CA 2598321A1 CA 002598321 A CA002598321 A CA 002598321A CA 2598321 A CA2598321 A CA 2598321A CA 2598321 A1 CA2598321 A1 CA 2598321A1
- Authority
- CA
- Canada
- Prior art keywords
- antibody
- biosample
- multimer
- epitope
- capturing
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 103
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 59
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 55
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 55
- 238000001514 detection method Methods 0.000 claims abstract description 49
- 230000015572 biosynthetic process Effects 0.000 claims abstract description 5
- 102000029797 Prion Human genes 0.000 claims description 136
- 108091000054 Prion Proteins 0.000 claims description 136
- 241000283690 Bos taurus Species 0.000 claims description 49
- 241000282414 Homo sapiens Species 0.000 claims description 41
- 210000004556 brain Anatomy 0.000 claims description 40
- 150000001413 amino acids Chemical group 0.000 claims description 38
- 235000001014 amino acid Nutrition 0.000 claims description 25
- 239000000758 substrate Substances 0.000 claims description 20
- 235000018102 proteins Nutrition 0.000 claims description 19
- 102000004169 proteins and genes Human genes 0.000 claims description 19
- 108090000623 proteins and genes Proteins 0.000 claims description 19
- 230000004520 agglutination Effects 0.000 claims description 18
- 239000011324 bead Substances 0.000 claims description 17
- 238000011282 treatment Methods 0.000 claims description 15
- 102000013566 Plasminogen Human genes 0.000 claims description 13
- 108010051456 Plasminogen Proteins 0.000 claims description 13
- 239000007787 solid Substances 0.000 claims description 12
- 239000003599 detergent Substances 0.000 claims description 11
- -1 .beta.-amyloid Proteins 0.000 claims description 10
- 108090000631 Trypsin Proteins 0.000 claims description 10
- 102000004142 Trypsin Human genes 0.000 claims description 10
- 239000003795 chemical substances by application Substances 0.000 claims description 10
- 229940016590 sarkosyl Drugs 0.000 claims description 10
- 108700004121 sarkosyl Proteins 0.000 claims description 10
- 239000012588 trypsin Substances 0.000 claims description 10
- 239000003112 inhibitor Substances 0.000 claims description 9
- 108050000761 Serpin Proteins 0.000 claims description 7
- 102000008847 Serpin Human genes 0.000 claims description 7
- 239000003001 serine protease inhibitor Substances 0.000 claims description 7
- 238000010438 heat treatment Methods 0.000 claims description 6
- 239000000126 substance Substances 0.000 claims description 6
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 5
- 108091005804 Peptidases Proteins 0.000 claims description 5
- 108010071690 Prealbumin Proteins 0.000 claims description 5
- 102000009190 Transthyretin Human genes 0.000 claims description 5
- 108010026424 tau Proteins Proteins 0.000 claims description 5
- 102000013498 tau Proteins Human genes 0.000 claims description 5
- 102000012192 Cystatin C Human genes 0.000 claims description 4
- 108010061642 Cystatin C Proteins 0.000 claims description 4
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 claims description 4
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 claims description 4
- 102000036770 Islet Amyloid Polypeptide Human genes 0.000 claims description 4
- 108010041872 Islet Amyloid Polypeptide Proteins 0.000 claims description 4
- 102000054727 Serum Amyloid A Human genes 0.000 claims description 4
- 108700028909 Serum Amyloid A Proteins 0.000 claims description 4
- 102000019197 Superoxide Dismutase Human genes 0.000 claims description 4
- 108010012715 Superoxide dismutase Proteins 0.000 claims description 4
- 239000002253 acid Substances 0.000 claims description 4
- WGQKYBSKWIADBV-UHFFFAOYSA-N benzylamine Chemical compound NCC1=CC=CC=C1 WGQKYBSKWIADBV-UHFFFAOYSA-N 0.000 claims description 4
- 238000002866 fluorescence resonance energy transfer Methods 0.000 claims description 4
- 239000004472 Lysine Substances 0.000 claims description 3
- 230000002255 enzymatic effect Effects 0.000 claims description 3
- 230000002285 radioactive effect Effects 0.000 claims description 3
- 235000019766 L-Lysine Nutrition 0.000 claims description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 claims description 2
- 229930064664 L-arginine Natural products 0.000 claims description 2
- 235000014852 L-arginine Nutrition 0.000 claims description 2
- 239000004365 Protease Substances 0.000 claims description 2
- 150000007513 acids Chemical class 0.000 claims description 2
- PXXJHWLDUBFPOL-UHFFFAOYSA-N benzamidine Chemical compound NC(=N)C1=CC=CC=C1 PXXJHWLDUBFPOL-UHFFFAOYSA-N 0.000 claims description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- KSAVQLQVUXSOCR-UHFFFAOYSA-M sodium lauroyl sarcosinate Chemical compound [Na+].CCCCCCCCCCCC(=O)N(C)CC([O-])=O KSAVQLQVUXSOCR-UHFFFAOYSA-M 0.000 claims 1
- 210000002381 plasma Anatomy 0.000 description 75
- 101710138751 Major prion protein Proteins 0.000 description 52
- 102100025818 Major prion protein Human genes 0.000 description 52
- 239000006180 TBST buffer Substances 0.000 description 24
- 208000008864 scrapie Diseases 0.000 description 24
- 239000000523 sample Substances 0.000 description 23
- 230000008569 process Effects 0.000 description 21
- 108010067770 Endopeptidase K Proteins 0.000 description 17
- 241000699666 Mus <mouse, genus> Species 0.000 description 16
- 238000011534 incubation Methods 0.000 description 16
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 14
- 241000699800 Cricetinae Species 0.000 description 13
- 229960002685 biotin Drugs 0.000 description 13
- 239000011616 biotin Substances 0.000 description 13
- SLXKOJJOQWFEFD-UHFFFAOYSA-N 6-aminohexanoic acid Chemical compound NCCCCCC(O)=O SLXKOJJOQWFEFD-UHFFFAOYSA-N 0.000 description 12
- 238000002965 ELISA Methods 0.000 description 12
- 229960002684 aminocaproic acid Drugs 0.000 description 12
- 239000000872 buffer Substances 0.000 description 11
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 11
- LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 description 10
- BACYUWVYYTXETD-UHFFFAOYSA-N N-Lauroylsarcosine Chemical compound CCCCCCCCCCCC(=O)N(C)CC(O)=O BACYUWVYYTXETD-UHFFFAOYSA-N 0.000 description 10
- 239000013504 Triton X-100 Substances 0.000 description 10
- 229920004890 Triton X-100 Polymers 0.000 description 10
- 230000027455 binding Effects 0.000 description 10
- 241001465754 Metazoa Species 0.000 description 9
- 201000010099 disease Diseases 0.000 description 9
- 208000003407 Creutzfeldt-Jakob Syndrome Diseases 0.000 description 8
- 208000024777 Prion disease Diseases 0.000 description 8
- 238000011161 development Methods 0.000 description 8
- 229920001213 Polysorbate 20 Polymers 0.000 description 7
- 235000020958 biotin Nutrition 0.000 description 7
- 230000029087 digestion Effects 0.000 description 7
- 229960000789 guanidine hydrochloride Drugs 0.000 description 7
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 7
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 7
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 7
- 208000020406 Creutzfeldt Jacob disease Diseases 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 108010090804 Streptavidin Proteins 0.000 description 6
- NZNMSOFKMUBTKW-UHFFFAOYSA-N cyclohexanecarboxylic acid Chemical compound OC(=O)C1CCCCC1 NZNMSOFKMUBTKW-UHFFFAOYSA-N 0.000 description 6
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 239000004816 latex Substances 0.000 description 6
- 229920000126 latex Polymers 0.000 description 6
- 230000003287 optical effect Effects 0.000 description 6
- 208000022256 primary systemic amyloidosis Diseases 0.000 description 6
- 208000010859 Creutzfeldt-Jakob disease Diseases 0.000 description 5
- 230000002776 aggregation Effects 0.000 description 5
- 238000004220 aggregation Methods 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 239000003398 denaturant Substances 0.000 description 5
- 229940009976 deoxycholate Drugs 0.000 description 5
- 229960003964 deoxycholic acid Drugs 0.000 description 5
- 238000003018 immunoassay Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 208000024827 Alzheimer disease Diseases 0.000 description 4
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 4
- 239000002033 PVDF binder Substances 0.000 description 4
- 102000035195 Peptidases Human genes 0.000 description 4
- 230000004931 aggregating effect Effects 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000000389 anti-prion effect Effects 0.000 description 4
- 238000000835 electrochemical detection Methods 0.000 description 4
- 230000036541 health Effects 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 4
- 206010014561 Emphysema Diseases 0.000 description 3
- 208000034846 Familial Amyloid Neuropathies Diseases 0.000 description 3
- 208000007487 Familial Cerebral Amyloid Angiopathy Diseases 0.000 description 3
- 206010016654 Fibrosis Diseases 0.000 description 3
- 201000011240 Frontotemporal dementia Diseases 0.000 description 3
- 206010019889 Hereditary neuropathic amyloidosis Diseases 0.000 description 3
- 208000023105 Huntington disease Diseases 0.000 description 3
- 208000005531 Immunoglobulin Light-chain Amyloidosis Diseases 0.000 description 3
- 208000018737 Parkinson disease Diseases 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 239000004793 Polystyrene Substances 0.000 description 3
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 3
- 230000002159 abnormal effect Effects 0.000 description 3
- 206010002022 amyloidosis Diseases 0.000 description 3
- 206010002026 amyotrophic lateral sclerosis Diseases 0.000 description 3
- 230000031016 anaphase Effects 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 230000007882 cirrhosis Effects 0.000 description 3
- 208000019425 cirrhosis of liver Diseases 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- VZFUCHSFHOYXIS-UHFFFAOYSA-N cycloheptane carboxylic acid Natural products OC(=O)C1CCCCCC1 VZFUCHSFHOYXIS-UHFFFAOYSA-N 0.000 description 3
- 230000007812 deficiency Effects 0.000 description 3
- 238000001378 electrochemiluminescence detection Methods 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 238000001631 haemodialysis Methods 0.000 description 3
- 238000011813 knockout mouse model Methods 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 230000009871 nonspecific binding Effects 0.000 description 3
- 239000002797 plasminogen activator inhibitor Substances 0.000 description 3
- 229920002223 polystyrene Polymers 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 235000019833 protease Nutrition 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 201000007905 transthyretin amyloidosis Diseases 0.000 description 3
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- 208000027121 wild type ATTR amyloidosis Diseases 0.000 description 3
- PKYCWFICOKSIHZ-UHFFFAOYSA-N 1-(3,7-dihydroxyphenoxazin-10-yl)ethanone Chemical compound OC1=CC=C2N(C(=O)C)C3=CC=C(O)C=C3OC2=C1 PKYCWFICOKSIHZ-UHFFFAOYSA-N 0.000 description 2
- ZBQCCTCQUCOXBO-UHFFFAOYSA-N 4-(4-aminophenyl)-2,2,6,6-tetramethylcyclohex-3-en-1-amine Chemical compound CC1(C)C(N)C(C)(C)CC(C=2C=CC(N)=CC=2)=C1 ZBQCCTCQUCOXBO-UHFFFAOYSA-N 0.000 description 2
- TUHVEAJXIMEOSA-UHFFFAOYSA-N 4-guanidinobutanoic acid Chemical compound NC(=[NH2+])NCCCC([O-])=O TUHVEAJXIMEOSA-UHFFFAOYSA-N 0.000 description 2
- JJMDCOVWQOJGCB-UHFFFAOYSA-N 5-aminopentanoic acid Chemical compound [NH3+]CCCCC([O-])=O JJMDCOVWQOJGCB-UHFFFAOYSA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 241000282994 Cervidae Species 0.000 description 2
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- SNEIUMQYRCDYCH-LURJTMIESA-N N(alpha)-acetyl-L-arginine Chemical compound CC(=O)N[C@H](C(O)=O)CCCNC(N)=N SNEIUMQYRCDYCH-LURJTMIESA-N 0.000 description 2
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 2
- 108010058846 Ovalbumin Proteins 0.000 description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- 208000002704 Sporadic Creutzfeldt-Jakob disease Diseases 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 208000018756 Variant Creutzfeldt-Jakob disease Diseases 0.000 description 2
- 235000010724 Wisteria floribunda Nutrition 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- XJMXIWNOKIEIMX-UHFFFAOYSA-N bromo chloro 1h-indol-2-yl phosphate Chemical compound C1=CC=C2NC(OP(=O)(OBr)OCl)=CC2=C1 XJMXIWNOKIEIMX-UHFFFAOYSA-N 0.000 description 2
- 239000004202 carbamide Substances 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- FPIQZBQZKBKLEI-UHFFFAOYSA-N ethyl 1-[[2-chloroethyl(nitroso)carbamoyl]amino]cyclohexane-1-carboxylate Chemical compound ClCCN(N=O)C(=O)NC1(C(=O)OCC)CCCCC1 FPIQZBQZKBKLEI-UHFFFAOYSA-N 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 2
- 229960004198 guanidine Drugs 0.000 description 2
- 229960002897 heparin Drugs 0.000 description 2
- 229920000669 heparin Polymers 0.000 description 2
- 230000016784 immunoglobulin production Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- IZWSFJTYBVKZNK-UHFFFAOYSA-N lauryl sulfobetaine Chemical compound CCCCCCCCCCCC[N+](C)(C)CCCS([O-])(=O)=O IZWSFJTYBVKZNK-UHFFFAOYSA-N 0.000 description 2
- KNJDBYZZKAZQNG-UHFFFAOYSA-N lucigenin Chemical compound [O-][N+]([O-])=O.[O-][N+]([O-])=O.C12=CC=CC=C2[N+](C)=C(C=CC=C2)C2=C1C1=C(C=CC=C2)C2=[N+](C)C2=CC=CC=C12 KNJDBYZZKAZQNG-UHFFFAOYSA-N 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000003068 molecular probe Substances 0.000 description 2
- 230000004770 neurodegeneration Effects 0.000 description 2
- 208000015122 neurodegenerative disease Diseases 0.000 description 2
- JPXMTWWFLBLUCD-UHFFFAOYSA-N nitro blue tetrazolium(2+) Chemical compound COC1=CC(C=2C=C(OC)C(=CC=2)[N+]=2N(N=C(N=2)C=2C=CC=CC=2)C=2C=CC(=CC=2)[N+]([O-])=O)=CC=C1[N+]1=NC(C=2C=CC=CC=2)=NN1C1=CC=C([N+]([O-])=O)C=C1 JPXMTWWFLBLUCD-UHFFFAOYSA-N 0.000 description 2
- 229940092253 ovalbumin Drugs 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 229910000160 potassium phosphate Inorganic materials 0.000 description 2
- 235000011009 potassium phosphates Nutrition 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 235000011149 sulphuric acid Nutrition 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000011534 wash buffer Substances 0.000 description 2
- AFDXODALSZRGIH-QPJJXVBHSA-N (E)-3-(4-methoxyphenyl)prop-2-enoic acid Chemical compound COC1=CC=C(\C=C\C(O)=O)C=C1 AFDXODALSZRGIH-QPJJXVBHSA-N 0.000 description 1
- AVQQQNCBBIEMEU-UHFFFAOYSA-N 1,1,3,3-tetramethylurea Chemical compound CN(C)C(=O)N(C)C AVQQQNCBBIEMEU-UHFFFAOYSA-N 0.000 description 1
- UCLKLGIYGBLTSM-UHFFFAOYSA-N 1,2,3,4-tetrachloro-5-(2,5-dichlorophenyl)benzene Chemical compound ClC1=CC=C(Cl)C(C=2C(=C(Cl)C(Cl)=C(Cl)C=2)Cl)=C1 UCLKLGIYGBLTSM-UHFFFAOYSA-N 0.000 description 1
- HWTAKVLMACWHLD-UHFFFAOYSA-N 2-(9h-carbazol-1-yl)ethanamine Chemical compound C12=CC=CC=C2NC2=C1C=CC=C2CCN HWTAKVLMACWHLD-UHFFFAOYSA-N 0.000 description 1
- KIUMMUBSPKGMOY-UHFFFAOYSA-N 3,3'-Dithiobis(6-nitrobenzoic acid) Chemical compound C1=C([N+]([O-])=O)C(C(=O)O)=CC(SSC=2C=C(C(=CC=2)[N+]([O-])=O)C(O)=O)=C1 KIUMMUBSPKGMOY-UHFFFAOYSA-N 0.000 description 1
- IITIZHOBOIBGBW-UHFFFAOYSA-N 3-ethyl-2h-1,3-benzothiazole Chemical compound C1=CC=C2N(CC)CSC2=C1 IITIZHOBOIBGBW-UHFFFAOYSA-N 0.000 description 1
- XDOLZJYETYVRKV-UHFFFAOYSA-N 7-Aminoheptanoic acid Chemical compound NCCCCCCC(O)=O XDOLZJYETYVRKV-UHFFFAOYSA-N 0.000 description 1
- 241000282979 Alces alces Species 0.000 description 1
- 108010039206 Biotinidase Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical group CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 208000003736 Gerstmann-Straussler-Scheinker Disease Diseases 0.000 description 1
- 206010072075 Gerstmann-Straussler-Scheinker syndrome Diseases 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- ZDLDXNCMJBOYJV-YFKPBYRVSA-N L-arginine, methyl ester Chemical compound COC(=O)[C@@H](N)CCCN=C(N)N ZDLDXNCMJBOYJV-YFKPBYRVSA-N 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 101001090203 Mus musculus Major prion protein Proteins 0.000 description 1
- 101100460719 Mus musculus Noto gene Proteins 0.000 description 1
- 101100298534 Mus musculus Prnp gene Proteins 0.000 description 1
- VEYYWZRYIYDQJM-ZETCQYMHSA-N N(2)-acetyl-L-lysine Chemical compound CC(=O)N[C@H](C([O-])=O)CCCC[NH3+] VEYYWZRYIYDQJM-ZETCQYMHSA-N 0.000 description 1
- 241000772415 Neovison vison Species 0.000 description 1
- 101100110224 Oreochromis mossambicus atp2b2 gene Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 101710131583 Trypsin-10 Proteins 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- SXEHKFHPFVVDIR-UHFFFAOYSA-N [4-(4-hydrazinylphenyl)phenyl]hydrazine Chemical compound C1=CC(NN)=CC=C1C1=CC=C(NN)C=C1 SXEHKFHPFVVDIR-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 208000005881 bovine spongiform encephalopathy Diseases 0.000 description 1
- HFNQLYDPNAZRCH-UHFFFAOYSA-N carbonic acid Chemical compound OC(O)=O.OC(O)=O HFNQLYDPNAZRCH-UHFFFAOYSA-N 0.000 description 1
- 150000007942 carboxylates Chemical class 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 208000017580 chronic wasting disease Diseases 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000012468 concentrated sample Substances 0.000 description 1
- 230000008876 conformational transition Effects 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 238000013399 early diagnosis Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 201000006061 fatal familial insomnia Diseases 0.000 description 1
- 210000003608 fece Anatomy 0.000 description 1
- 208000037957 feline spongiform encephalopathy Diseases 0.000 description 1
- 108010073651 fibrinmonomer Proteins 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 229960003692 gamma aminobutyric acid Drugs 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- 208000027488 iatrogenic Creutzfeldt-Jakob disease Diseases 0.000 description 1
- 230000000642 iatrogenic effect Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 230000001524 infective effect Effects 0.000 description 1
- 208000019715 inherited Creutzfeldt-Jakob disease Diseases 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 206010023497 kuru Diseases 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 235000018977 lysine Nutrition 0.000 description 1
- 238000007433 macroscopic evaluation Methods 0.000 description 1
- 230000007257 malfunction Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- KPNBUPJZFJCCIQ-LURJTMIESA-N methyl L-lysinate Chemical compound COC(=O)[C@@H](N)CCCCN KPNBUPJZFJCCIQ-LURJTMIESA-N 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 230000007171 neuropathology Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000007500 overflow downdraw method Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 239000000700 radioactive tracer Substances 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 210000000582 semen Anatomy 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical class [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 229940045136 urea Drugs 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 239000002888 zwitterionic surfactant Substances 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Chemical & Material Sciences (AREA)
- Urology & Nephrology (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Neurosurgery (AREA)
- Neurology (AREA)
- Food Science & Technology (AREA)
- Cell Biology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| KR20050013877 | 2005-02-19 | ||
| KR10-2005-0013877 | 2005-02-19 | ||
| KRPCT/KR2005/000733 | 2005-03-11 | ||
| KR2005000733 | 2005-03-11 | ||
| PCT/KR2005/004001 WO2006088281A1 (fr) | 2005-02-19 | 2005-11-25 | Procede de detection differentielle d'une forme multimere a partir d'une forme monomere de polypeptides formant des multimeres |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2598321A1 true CA2598321A1 (fr) | 2006-08-24 |
Family
ID=36916659
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002598321A Abandoned CA2598321A1 (fr) | 2005-02-19 | 2005-11-25 | Procede de detection differentielle d'une forme multimere a partir d'une forme monomere de polypeptides formant des multimeres |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US8026070B2 (fr) |
| EP (1) | EP1848817B1 (fr) |
| JP (1) | JP4772065B2 (fr) |
| KR (2) | KR20100087403A (fr) |
| AU (1) | AU2005327652A1 (fr) |
| CA (1) | CA2598321A1 (fr) |
| WO (1) | WO2006088281A1 (fr) |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050026165A1 (en) * | 2001-05-31 | 2005-02-03 | Cindy Orser | Detection of conformationally altered proteins and prions |
| WO2007123345A1 (fr) * | 2006-04-21 | 2007-11-01 | Peoplebio, Inc. | Procédé de détection différentielle d'une forme multimère et d'une forme monomère dans des polypeptides formant des multimères par interactions tridimensionnelles |
| GB0611708D0 (en) * | 2006-06-14 | 2006-07-26 | Common Services Agency | Novel antibodies against prion protein and uses thereof |
| US7851172B2 (en) * | 2006-07-25 | 2010-12-14 | University Of Kentucky Research Foundation | Biomarkers of mild cognitive impairment and alzheimer's disease |
| JP2010523977A (ja) * | 2007-04-04 | 2010-07-15 | ノバルティス アーゲー | プリオンアッセイ |
| CA2684798A1 (fr) * | 2007-04-04 | 2008-10-16 | Novartis Ag | Dosage immuno-enzymatique (elisa) du prion |
| GB0718603D0 (en) * | 2007-09-24 | 2007-10-31 | Medical Res Council | Methods |
| JP5368284B2 (ja) * | 2009-12-10 | 2013-12-18 | 独立行政法人科学技術振興機構 | アミロイド凝集体の検出試薬及び検出方法 |
| SG10201708959WA (en) | 2012-07-03 | 2017-11-29 | Univ Washington | Antibodies to tau |
| KR101451797B1 (ko) * | 2012-11-07 | 2014-10-16 | 가천대학교 산학협력단 | 멀티머-형성 폴리펩타이드의 멀티머 정량분석을 위한 표준 단백질 복합체 |
| DE102013106713A1 (de) * | 2013-06-26 | 2014-12-31 | Forschungszentrum Jülich GmbH | Verfahren zur Ermittlung von Indikatoren zur Bestimmung von Krankheiten |
| TWI734975B (zh) | 2014-06-27 | 2021-08-01 | 美商Ｃ２Ｎ醫療診斷有限責任公司 | 人類化抗-tau抗體 |
| KR101658620B1 (ko) * | 2014-12-02 | 2016-09-23 | 주식회사 피플바이오 | 응집형-형성 폴리펩타이드의 응집형을 검출하는 방법 |
| EP3415912B1 (fr) | 2016-02-08 | 2023-03-29 | Sysmex Corporation | Méthode de détection d'analyte et kit de réactifs permettant de détecter un analyte |
| KR20170108203A (ko) * | 2016-03-16 | 2017-09-27 | 주식회사 피플바이오 | 응집형-형성 폴리펩타이드의 응집형을 검출하는 방법 |
| KR101871895B1 (ko) * | 2016-04-20 | 2018-06-28 | 한국과학기술연구원 | 응집 단백질의 고감도 광 산화 증폭 면역 분석을 통한 체액기반의 퇴행성 신경질환 진단 방법 |
| ITUA20163473A1 (it) * | 2016-05-16 | 2017-11-16 | Univ Pisa | Metodo per la diagnosi di malattie neurodegenerative |
| JP6883847B2 (ja) * | 2017-03-30 | 2021-06-09 | 国立大学法人滋賀医科大学 | アミロイドβ蛋白並びにタウ蛋白及び／又はリン酸化タウ蛋白の測定方法 |
| US12115141B2 (en) | 2018-11-14 | 2024-10-15 | University Of Kentucky Research Foundation | Diagnosis of diabetes by detecting aggregated amylin in erythrocytes |
| WO2022226731A1 (fr) * | 2021-04-26 | 2022-11-03 | 北京盛美诺生物技术有限公司 | Procédé de prétraitement pour la détection quantitative de collagène de type ii non dénaturé dans un produit de collagène ou un cartilage et application |
| WO2025096519A1 (fr) * | 2023-10-31 | 2025-05-08 | Illumina, Inc. | Biocapteur transducteur non volatil programmable par des ions à haute densité |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2681370B2 (ja) * | 1988-06-30 | 1997-11-26 | 塩野義製薬株式会社 | 免疫測定法 |
| FR2774988B1 (fr) * | 1998-02-16 | 2000-05-05 | Commissariat Energie Atomique | Procede de purification de la prpres a partir d'un echantillon biologique et ses applications |
| US6750025B1 (en) | 1998-07-09 | 2004-06-15 | V.I. Technologies, Inc. | Method of detecting and isolating prion protein and variants thereof |
| US6972198B2 (en) | 1999-02-26 | 2005-12-06 | Cyclacel, Ltd. | Methods and compositions using protein binding partners |
| US6846640B2 (en) * | 2002-04-30 | 2005-01-25 | Pharmacia & Upjohn Company | Time-resolved fluorescence assay for the detection of multimeric forms of A-beta 1-40 |
| US20070077603A1 (en) * | 2005-07-12 | 2007-04-05 | Heeb Mary J | Elisa to detect multimeric forms of a protein |
-
2005
- 2005-11-25 CA CA002598321A patent/CA2598321A1/fr not_active Abandoned
- 2005-11-25 WO PCT/KR2005/004001 patent/WO2006088281A1/fr not_active Ceased
- 2005-11-25 EP EP05819063.8A patent/EP1848817B1/fr not_active Expired - Lifetime
- 2005-11-25 KR KR1020107014229A patent/KR20100087403A/ko not_active Ceased
- 2005-11-25 JP JP2007556064A patent/JP4772065B2/ja not_active Expired - Lifetime
- 2005-11-25 KR KR1020107001057A patent/KR20100036324A/ko not_active Ceased
- 2005-11-25 AU AU2005327652A patent/AU2005327652A1/en not_active Abandoned
- 2005-11-25 US US11/816,261 patent/US8026070B2/en active Active
Also Published As
| Publication number | Publication date |
|---|---|
| JP2008530578A (ja) | 2008-08-07 |
| EP1848817B1 (fr) | 2013-04-24 |
| JP4772065B2 (ja) | 2011-09-14 |
| KR20100087403A (ko) | 2010-08-04 |
| AU2005327652A1 (en) | 2006-08-24 |
| US8026070B2 (en) | 2011-09-27 |
| EP1848817A4 (fr) | 2008-09-10 |
| US20100009388A1 (en) | 2010-01-14 |
| EP1848817A1 (fr) | 2007-10-31 |
| KR20100036324A (ko) | 2010-04-07 |
| WO2006088281A1 (fr) | 2006-08-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8026070B2 (en) | Differential detection of multimeric and monomeric forms of multimer-forming polypeptides | |
| US8008026B2 (en) | Methods for differentially detecting a multimeric form from a monomeric form of a multimer-forming polypeptide through three-dimensional interactions | |
| JP6275869B2 (ja) | 関節リウマチの診断のための組成物及び方法 | |
| KR100987639B1 (ko) | 멀티머-형성 폴리펩타이드의 모노머로부터 멀티머를 분별검출하는 방법 | |
| KR100979070B1 (ko) | 사람 기원의 병원성 프리온을 특이적으로 검출하는 항체및 당해 항체를 사용하여 수행되는 검출 방법 | |
| JP2018503807A (ja) | 凝集形−形成ポリペプチドの凝集形を検出する方法 | |
| US20080057523A1 (en) | Detection of Protein Aggregates by Homologous Elisa | |
| JP6745351B2 (ja) | 凝集型−形成ポリペプチドの凝集型を検出する方法 | |
| EP1462804A1 (fr) | Méthode de détection de la forme pathogene de protéines prion | |
| WO2009011500A2 (fr) | Procédés pour diminuer de faux signaux dans un essai immunologique pour détecter une forme multimère d'une forme monomère de polypeptides formant des multimères | |
| CN101427132A (zh) | 通过三维相互作用从多聚体形成多肽的单体形式中示差检测多聚体形式的方法 | |
| WO2008029965A1 (fr) | Dosage de réaction simultané destiné à détecter de façon différentielle une forme multimère | |
| JP3768165B2 (ja) | 抗カルパスタチン抗体の測定法及び測定キット | |
| US20090162943A1 (en) | Reagents and Methods for the Detection of Transmissible Spongiform Encephalopathy | |
| KR20060025296A (ko) | 정상형 프라이온에 대한 항체 및 그의 용도 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |